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Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.

ABSTRACT: Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described. Crystals grown in the presence of high-molecular-weight PEG precipitant and magnesium chloride were found to diffract beyond 1.65?Å resolution. The crystal lattice belonged to the hexagonal space group P6?22, with unit-cell parameters a=b=89.31, c=290.18?Å, and contained two molecules in the asymmetric unit. The crystal structure was determined by molecular replacement using a single chain of Pseudomonas aeruginosa DHDPS as the search model.

SUBMITTER: Siddiqui T

PROVIDER: S-EPMC3792684 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.

Siddiqui Tanzeela T Paxman Jason J JJ Dogovski Con C Panjikar Santosh S Perugini Matthew A MA

Acta crystallographica. Section F, Structural biology and crystallization communications 20130930 Pt 10

Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described. Crystals grown in the presence of high-molecular-weight PEG precipitant and magnesium chloride were found to diffract beyond 1.65 Å resolution. The crystal lattice belonged to the hexagonal space group P6₁22, with unit-cell paramet ...[more]

PMID: 24100576

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